ID HG2A_HUMAN Reviewed; 296 AA.
AC P04233; A8K7R1; B4DNE8; D3DQG3; D3DQG4; Q14597; Q29832; Q5U0J8; Q8SNA0;
AC Q8WLP6;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 3.
DT 27-MAR-2024, entry version 240.
DE RecName: Full=HLA class II histocompatibility antigen gamma chain {ECO:0000305};
DE AltName: Full=HLA-DR antigens-associated invariant chain;
DE AltName: Full=Ia antigen-associated invariant chain;
DE Short=Ii;
DE AltName: CD_antigen=CD74;
DE Contains:
DE RecName: Full=Class-II-associated invariant chain peptide {ECO:0000303|PubMed:1448172};
DE Short=CLIP {ECO:0000303|PubMed:1448172};
GN Name=CD74 {ECO:0000312|HGNC:HGNC:1697}; Synonyms=DHLAG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P35).
RX PubMed=6324166; DOI=10.1073/pnas.80.24.7395;
RA Claesson L., Larhammar D., Rask L., Peterson P.A.;
RT "cDNA clone for the human invariant gamma chain of class II
RT histocompatibility antigens and its implications for the protein
RT structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:7395-7399(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P35).
RX PubMed=6586420; DOI=10.1002/j.1460-2075.1984.tb01898.x;
RA Strubin M., Mach B., Long E.O.;
RT "The complete sequence of the mRNA for the HLA-DR-associated invariant
RT chain reveals a polypeptide with an unusual transmembrane polarity.";
RL EMBO J. 3:869-872(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM P35).
RX PubMed=3001652; DOI=10.1093/nar/13.24.8827;
RA Kudo J., Chao L.-Y., Narni F., Saunders G.F.;
RT "Structure of the human gene encoding the invariant gamma-chain of class II
RT histocompatibility antigens.";
RL Nucleic Acids Res. 13:8827-8841(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS P45
RP AND P35).
RC TISSUE=Liver;
RX PubMed=3459184; DOI=10.1073/pnas.83.12.4484;
RA O'Sullivan D.M., Larhammar D., Wilson M.C., Peterson P.A., Quaranta V.;
RT "Structure of the human Ia-associated invariant (gamma)-chain gene:
RT identification of 5' sequences shared with major histocompatibility complex
RT class II genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4484-4488(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P35).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P45 AND P35).
RC TISSUE=Heart, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P35 AND 3).
RC TISSUE=B-cell, and Tonsil;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 22-35; 81-94; 171-179 AND 273-288, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 97-120, AND FUNCTION.
RX PubMed=1448172; DOI=10.1038/360474a0;
RA Riberdy J.M., Newcomb J.R., Surman M.J., Barbosa J.A., Cresswell P.;
RT "HLA-DR molecules from an antigen-processing mutant cell line are
RT associated with invariant chain peptides.";
RL Nature 360:474-477(1992).
RN [12]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=3104027; DOI=10.1002/j.1460-2075.1986.tb04673.x;
RA Strubin M., Berte C., Mach B.;
RT "Alternative splicing and alternative initiation of translation explain the
RT four forms of the Ia antigen-associated invariant chain.";
RL EMBO J. 5:3483-3488(1986).
RN [13]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH ROS1.
RX PubMed=12661006; DOI=10.1002/gcc.10207;
RA Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H.,
RA Housman D.;
RT "Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma with
RT an interstitial del(6)(q21q21).";
RL Genes Chromosomes Cancer 37:58-71(2003).
RN [14]
RP INTERACTION WITH MIF.
RX PubMed=12782713; DOI=10.1084/jem.20030286;
RA Leng L., Metz C.N., Fang Y., Xu J., Donnelly S., Baugh J., Delohery T.,
RA Chen Y., Mitchell R.A., Bucala R.;
RT "MIF signal transduction initiated by binding to CD74.";
RL J. Exp. Med. 197:1467-1476(2003).
RN [15]
RP REVIEW.
RX PubMed=19092054; DOI=10.1242/jcs.035089;
RA Berger A.C., Roche P.A.;
RT "MHC class II transport at a glance.";
RL J. Cell Sci. 122:1-4(2009).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP GLYCOSYLATION AT THR-203, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [19]
RP GLYCOSYLATION AT THR-203 AND SER-281, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [20]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-282.
RX PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA Nilsson J., Larson G.;
RT "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT prohormones as a novel class of proteoglycans.";
RL Mol. Cell. Proteomics 14:41-49(2015).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP GLYCOSYLATION AT SER-282.
RX PubMed=32337544; DOI=10.1093/glycob/cwaa039;
RA Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A.,
RA Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D.,
RA Larson G., Salanti A., Clausen T.M.;
RT "An affinity chromatography and glycoproteomics workflow to profile the
RT chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in
RT the placenta and in cancer.";
RL Glycobiology 30:989-1002(2020).
RN [23]
RP FUNCTION (ISOFORM P41), ALTERNATIVE SPLICING, AND MUTAGENESIS OF
RP 225-PRO-GLY-226.
RX PubMed=32855215; DOI=10.1126/science.abb3753;
RA Bruchez A., Sha K., Johnson J., Chen L., Stefani C., McConnell H.,
RA Gaucherand L., Prins R., Matreyek K.A., Hume A.J., Muehlberger E.,
RA Schmidt E.V., Olinger G.G., Stuart L.M., Lacy-Hulbert A.;
RT "MHC class II transactivator CIITA induces cell resistance to Ebola virus
RT and SARS-like coronaviruses.";
RL Science 370:241-247(2020).
RN [24]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-282.
RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3;
RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K.,
RA Pandey A.;
RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides.";
RL J. Proteins Proteom. 13:187-203(2022).
RN [25]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-282.
RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617;
RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.;
RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected
RT Correlation Between Glycan Sulfation and Attachment Site Characteristics.";
RL Mol. Cell. Proteomics 22:100617-100617(2023).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 103-117 (CLIP) IN COMPLEX WITH
RP HLA-DRA/HLA-DRB1 HETERODIMER.
RX PubMed=7477400; DOI=10.1038/378457a0;
RA Ghosh P., Amaya M., Mellins E., Wiley D.C.;
RT "The structure of an intermediate in class II MHC maturation: CLIP bound to
RT HLA-DR3.";
RL Nature 378:457-462(1995).
RN [27]
RP STRUCTURE BY NMR OF 134-208.
RX PubMed=9843486; DOI=10.1093/emboj/17.23.6812;
RA Jasanoff A., Wagner G., Wiley D.C.;
RT "Structure of a trimeric domain of the MHC class II-associated chaperonin
RT and targeting protein Ii.";
RL EMBO J. 17:6812-6818(1998).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 210-274, GLYCOSYLATION AT ASN-256,
RP DISULFIDE BONDS, AND INTERACTION WITH CTSL.
RX PubMed=10022822; DOI=10.1093/emboj/18.4.793;
RA Guncar G., Pungercic G., Klemencic I., Turk V., Turk D.;
RT "Crystal structure of MHC class II-associated p41 Ii fragment bound to
RT cathepsin L reveals the structural basis for differentiation between
RT cathepsins L and S.";
RL EMBO J. 18:793-803(1999).
CC -!- FUNCTION: Plays a critical role in MHC class II antigen processing by
CC stabilizing peptide-free class II alpha/beta heterodimers in a complex
CC soon after their synthesis and directing transport of the complex from
CC the endoplasmic reticulum to the endosomal/lysosomal system where the
CC antigen processing and binding of antigenic peptides to MHC class II
CC takes place. Serves as cell surface receptor for the cytokine MIF.
CC -!- FUNCTION: [Class-II-associated invariant chain peptide]: Binds to the
CC peptide-binding site of MHC class II alpha/beta heterodimers forming an
CC alpha-beta-CLIP complex, thereby preventing the loading of antigenic
CC peptides to the MHC class II complex until its release by HLA-DM in the
CC endosome. {ECO:0000269|PubMed:1448172}.
CC -!- FUNCTION: [Isoform p41]: Stabilizes the conformation of mature CTSL by
CC binding to its active site and serving as a chaperone to help maintain
CC a pool of mature enzyme in endocytic compartments and extracellular
CC space of antigen-presenting cells (APCs). Has antiviral activity by
CC stymieing the endosomal entry of Ebola virus and coronaviruses,
CC including SARS-CoV-2 (PubMed:32855215). Disrupts cathepsin-mediated
CC Ebola virus glycoprotein processing, which prevents viral fusion and
CC entry. This antiviral activity is specific to p41 isoform
CC (PubMed:32855215). {ECO:0000250|UniProtKB:P04441,
CC ECO:0000269|PubMed:32855215}.
CC -!- SUBUNIT: Homotrimer. In the endoplasmic reticulum (ER) it forms a
CC heterononameric MHC II-Ii complex: 3 MHC class II molecules
CC (heterodimers of an alpha and a beta subunit) bind to the CD74
CC homotrimer (also known as invariant chain or HLA class II
CC histocompatibility antigen gamma chain). In the endosomal/lysosomal
CC system, the CD74 component undergoes sequential degradation by various
CC proteases, including CTSS and CTSL, leaving a small fragment termed
CC CLIP (class-II-associated invariant chain peptide) attached to the MHC
CC class II molecule (alpha-beta-CLIP complex). This processed complex
CC interacts with HLA_DM and HLA_DO heterodimers in order to release CLIP
CC and facilitate the binding of antigenic peptides to the MHC class II
CC molecules. Interacts with CD44; this complex is essential for the MIF-
CC induced signaling cascade that results in B cell survival.
CC {ECO:0000250|UniProtKB:P04441, ECO:0000269|PubMed:12782713,
CC ECO:0000269|PubMed:7477400}.
CC -!- SUBUNIT: [Isoform p41]: Interacts with the mature form of CTSL; the
CC complex survive in neutral pH environment.
CC {ECO:0000269|PubMed:10022822}.
CC -!- INTERACTION:
CC P04233; P16070: CD44; NbExp=9; IntAct=EBI-2622890, EBI-490245;
CC P04233; P25025: CXCR2; NbExp=2; IntAct=EBI-2622890, EBI-2835281;
CC P04233; P61073: CXCR4; NbExp=4; IntAct=EBI-2622890, EBI-489411;
CC P04233; P60228: EIF3E; NbExp=2; IntAct=EBI-2622890, EBI-347740;
CC P04233; Q14974: KPNB1; NbExp=2; IntAct=EBI-2622890, EBI-286758;
CC P04233; P0A6Y8: dnaK; Xeno; NbExp=8; IntAct=EBI-2622890, EBI-542092;
CC P04233-2; O15155: BET1; NbExp=3; IntAct=EBI-12222807, EBI-749204;
CC P04233-2; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-12222807, EBI-12256978;
CC P04233-2; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-12222807, EBI-11989440;
CC P04233-2; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-12222807, EBI-2807956;
CC P04233-2; P56851: EDDM3B; NbExp=3; IntAct=EBI-12222807, EBI-10215665;
CC P04233-2; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12222807, EBI-711490;
CC P04233-2; P37268: FDFT1; NbExp=3; IntAct=EBI-12222807, EBI-714550;
CC P04233-2; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-12222807, EBI-713304;
CC P04233-2; Q9UBY5: LPAR3; NbExp=4; IntAct=EBI-12222807, EBI-12033434;
CC P04233-2; Q8N912: NRAC; NbExp=4; IntAct=EBI-12222807, EBI-12051377;
CC P04233-2; P0DJD7: PGA4; NbExp=3; IntAct=EBI-12222807, EBI-12957629;
CC P04233-2; P60201-2: PLP1; NbExp=3; IntAct=EBI-12222807, EBI-12188331;
CC P04233-2; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-12222807, EBI-10485931;
CC P04233-2; Q8WZA1: POMGNT1; NbExp=3; IntAct=EBI-12222807, EBI-3912424;
CC P04233-2; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-12222807, EBI-14199621;
CC P04233-2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-12222807, EBI-10244780;
CC P04233-2; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12222807, EBI-8652744;
CC P04233-2; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-12222807, EBI-10329948;
CC P04233-2; P78383: SLC35B1; NbExp=3; IntAct=EBI-12222807, EBI-12147661;
CC P04233-2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-12222807, EBI-12188413;
CC P04233-2; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-12222807, EBI-11523345;
CC P04233-2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-12222807, EBI-10171534;
CC P04233-2; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-12222807, EBI-12887458;
CC P04233-2; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-12222807, EBI-11956809;
CC P04233-2; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-12222807, EBI-2852148;
CC P04233-2; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12222807, EBI-12111910;
CC P04233-2; O00526: UPK2; NbExp=4; IntAct=EBI-12222807, EBI-10179682;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane. Golgi
CC apparatus, trans-Golgi network. Endosome. Lysosome. Secreted
CC {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313,
CC ECO:0000269|PubMed:37453717}. Note=Transits through a number of
CC intracellular compartments in the endocytic pathway. It can either
CC undergo proteolysis or reach the cell membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform p41]: Late endosome
CC {ECO:0000250|UniProtKB:P04441}. Lysosome
CC {ECO:0000250|UniProtKB:P04441}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC Name=p45 {ECO:0000303|PubMed:3104027}; Synonyms=Long;
CC IsoId=P04233-1; Sequence=Displayed;
CC Name=p35 {ECO:0000303|PubMed:3104027}; Synonyms=Short;
CC IsoId=P04233-2; Sequence=VSP_005331;
CC Name=3;
CC IsoId=P04233-3; Sequence=VSP_037869, VSP_037870;
CC Name=p41 {ECO:0000303|PubMed:3104027};
CC IsoId=P04233-4; Sequence=VSP_060904;
CC Name=p33 {ECO:0000303|PubMed:3104027};
CC IsoId=P04233-5; Sequence=VSP_060904, VSP_005331;
CC -!- TISSUE SPECIFICITY: Detected in urine (at protein level).
CC {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313,
CC ECO:0000269|PubMed:37453717}.
CC -!- TISSUE SPECIFICITY: [Isoform p41]: In B cells, represents 10% of total
CC CD74 expression. {ECO:0000269|PubMed:3104027}.
CC -!- TISSUE SPECIFICITY: [Isoform p33]: In B cells, represents 70% of total
CC CD74 expression. {ECO:0000269|PubMed:3104027}.
CC -!- DOMAIN: Antiviral activity requires delivery of the thyroglobulin
CC domain to the endosomal membrane. {ECO:0000269|PubMed:32855215}.
CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans
CC (PubMed:22171320, PubMed:23234360). Contains chondroitin sulfate
CC (PubMed:25326458). {ECO:0000269|PubMed:22171320,
CC ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:25326458}.
CC -!- DISEASE: Note=A chromosomal aberration involving CD74 is found in a
CC non-small cell lung tumor. Results in the formation of a CD74-ROS1
CC chimeric protein. {ECO:0000269|PubMed:12661006}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36304.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; K01144; AAA36304.1; ALT_INIT; mRNA.
DR EMBL; X00497; CAA25192.1; -; mRNA.
DR EMBL; X00497; CAA25193.1; -; mRNA.
DR EMBL; X03339; CAA27046.1; -; Genomic_DNA.
DR EMBL; X03340; CAA27047.1; -; Genomic_DNA.
DR EMBL; M13560; AAA36033.1; -; Genomic_DNA.
DR EMBL; M13555; AAA36033.1; JOINED; Genomic_DNA.
DR EMBL; M13556; AAA36033.1; JOINED; Genomic_DNA.
DR EMBL; M13558; AAA36033.1; JOINED; Genomic_DNA.
DR EMBL; M13559; AAA36033.1; JOINED; Genomic_DNA.
DR EMBL; BT019505; AAV38312.1; -; mRNA.
DR EMBL; AK292076; BAF84765.1; -; mRNA.
DR EMBL; AK297889; BAG60210.1; -; mRNA.
DR EMBL; AC011372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61727.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61728.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61729.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61730.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61731.1; -; Genomic_DNA.
DR EMBL; BC018726; AAH18726.1; -; mRNA.
DR EMBL; BC024272; AAH24272.1; -; mRNA.
DR CCDS; CCDS34276.1; -. [P04233-3]
DR CCDS; CCDS47308.1; -. [P04233-2]
DR CCDS; CCDS47309.1; -. [P04233-1]
DR PIR; A93981; HLHUG.
DR RefSeq; NP_001020329.1; NM_001025158.2. [P04233-3]
DR RefSeq; NP_001020330.1; NM_001025159.2. [P04233-1]
DR RefSeq; NP_004346.1; NM_004355.3. [P04233-2]
DR PDB; 1A6A; X-ray; 2.75 A; C=103-117.
DR PDB; 1ICF; X-ray; 2.00 A; I/J=210-274.
DR PDB; 1IIE; NMR; -; A/B/C=134-208.
DR PDB; 1L3H; NMR; -; A=210-274.
DR PDB; 1MUJ; X-ray; 2.15 A; C=97-121.
DR PDB; 3PDO; X-ray; 1.95 A; C=102-120.
DR PDB; 3PGC; X-ray; 2.66 A; C/F=106-120.
DR PDB; 3PGD; X-ray; 2.72 A; C/F=106-120.
DR PDB; 3QXA; X-ray; 2.71 A; C/F=103-117.
DR PDB; 3QXD; X-ray; 2.30 A; C/F=103-117.
DR PDB; 4AEN; X-ray; 2.20 A; C=106-120.
DR PDB; 4AH2; X-ray; 2.36 A; B=106-120.
DR PDB; 4X5W; X-ray; 1.34 A; C=102-120.
DR PDB; 5KSU; X-ray; 2.73 A; C/F=103-117.
DR PDB; 5KSV; X-ray; 2.19 A; C=109-123.
DR PDB; 7YX9; X-ray; 1.76 A; E/G=103-117.
DR PDB; 7YXB; X-ray; 2.10 A; G/H=103-117.
DR PDB; 7Z0Q; X-ray; 2.10 A; G=103-117.
DR PDBsum; 1A6A; -.
DR PDBsum; 1ICF; -.
DR PDBsum; 1IIE; -.
DR PDBsum; 1L3H; -.
DR PDBsum; 1MUJ; -.
DR PDBsum; 3PDO; -.
DR PDBsum; 3PGC; -.
DR PDBsum; 3PGD; -.
DR PDBsum; 3QXA; -.
DR PDBsum; 3QXD; -.
DR PDBsum; 4AEN; -.
DR PDBsum; 4AH2; -.
DR PDBsum; 4X5W; -.
DR PDBsum; 5KSU; -.
DR PDBsum; 5KSV; -.
DR PDBsum; 7YX9; -.
DR PDBsum; 7YXB; -.
DR PDBsum; 7Z0Q; -.
DR AlphaFoldDB; P04233; -.
DR BMRB; P04233; -.
DR SMR; P04233; -.
DR BioGRID; 107410; 145.
DR ELM; P04233; -.
DR IntAct; P04233; 200.
DR MINT; P04233; -.
DR STRING; 9606.ENSP00000009530; -.
DR BindingDB; P04233; -.
DR ChEMBL; CHEMBL4692; -.
DR GuidetoPHARMACOLOGY; 2840; -.
DR MEROPS; I31.002; -.
DR TCDB; 9.A.75.1.1; the mhc ii receptor (mhc2r) family.
DR GlyConnect; 659; 11 N-Linked glycans (2 sites), 1 O-Linked glycan (1 site).
DR GlyCosmos; P04233; 8 sites, 14 glycans.
DR GlyGen; P04233; 12 sites, 11 N-linked glycans (2 sites), 4 O-linked glycans (7 sites).
DR iPTMnet; P04233; -.
DR PhosphoSitePlus; P04233; -.
DR SwissPalm; P04233; -.
DR BioMuta; CD74; -.
DR DMDM; 20178292; -.
DR CPTAC; CPTAC-5941; -.
DR EPD; P04233; -.
DR jPOST; P04233; -.
DR MassIVE; P04233; -.
DR MaxQB; P04233; -.
DR PaxDb; 9606-ENSP00000009530; -.
DR PeptideAtlas; P04233; -.
DR ProteomicsDB; 51689; -. [P04233-1]
DR ProteomicsDB; 51690; -. [P04233-2]
DR ProteomicsDB; 51691; -. [P04233-3]
DR Pumba; P04233; -.
DR ABCD; P04233; 19 sequenced antibodies.
DR Antibodypedia; 2245; 2682 antibodies from 53 providers.
DR CPTC; P04233; 1 antibody.
DR DNASU; 972; -.
DR Ensembl; ENST00000009530.13; ENSP00000009530.7; ENSG00000019582.17. [P04233-1]
DR Ensembl; ENST00000353334.11; ENSP00000230685.6; ENSG00000019582.17. [P04233-2]
DR Ensembl; ENST00000377795.7; ENSP00000367026.3; ENSG00000019582.17. [P04233-3]
DR GeneID; 972; -.
DR KEGG; hsa:972; -.
DR MANE-Select; ENST00000009530.13; ENSP00000009530.7; NM_001025159.3; NP_001020330.1.
DR UCSC; uc003lsc.4; human. [P04233-1]
DR AGR; HGNC:1697; -.
DR CTD; 972; -.
DR DisGeNET; 972; -.
DR GeneCards; CD74; -.
DR HGNC; HGNC:1697; CD74.
DR HPA; ENSG00000019582; Tissue enhanced (lymphoid).
DR MIM; 142790; gene.
DR neXtProt; NX_P04233; -.
DR OpenTargets; ENSG00000019582; -.
DR PharmGKB; PA26236; -.
DR VEuPathDB; HostDB:ENSG00000019582; -.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00390000008961; -.
DR InParanoid; P04233; -.
DR OMA; HHNCSEP; -.
DR OrthoDB; 2972165at2759; -.
DR PhylomeDB; P04233; -.
DR TreeFam; TF317779; -.
DR PathwayCommons; P04233; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR SignaLink; P04233; -.
DR SIGNOR; P04233; -.
DR BioGRID-ORCS; 972; 13 hits in 1159 CRISPR screens.
DR ChiTaRS; CD74; human.
DR EvolutionaryTrace; P04233; -.
DR GeneWiki; CD74; -.
DR GenomeRNAi; 972; -.
DR Pharos; P04233; Tchem.
DR PRO; PR:P04233; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P04233; Protein.
DR Bgee; ENSG00000019582; Expressed in monocyte and 202 other cell types or tissues.
DR ExpressionAtlas; P04233; baseline and differential.
DR Genevisible; P04233; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0042613; C:MHC class II protein complex; ISS:BHF-UCL.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0035693; C:NOS2-CD74 complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR GO; GO:0005773; C:vacuole; IDA:BHF-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:BHF-UCL.
DR GO; GO:0042609; F:CD4 receptor binding; IPI:CAFA.
DR GO; GO:0019955; F:cytokine binding; IPI:BHF-UCL.
DR GO; GO:0004896; F:cytokine receptor activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; TAS:UniProtKB.
DR GO; GO:0035718; F:macrophage migration inhibitory factor binding; IPI:BHF-UCL.
DR GO; GO:0042289; F:MHC class II protein binding; ISS:BHF-UCL.
DR GO; GO:0042658; F:MHC class II protein binding, via antigen binding groove; IDA:UniProtKB.
DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IBA:GO_Central.
DR GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; NAS:UniProtKB.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:Ensembl.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0035691; P:macrophage migration inhibitory factor signaling pathway; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0002792; P:negative regulation of peptide secretion; IDA:BHF-UCL.
DR GO; GO:0045581; P:negative regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:CAFA.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISS:BHF-UCL.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:ARUK-UCL.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:CAFA.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:ARUK-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:ARUK-UCL.
DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:CAFA.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISS:BHF-UCL.
DR GO; GO:2000448; P:positive regulation of macrophage migration inhibitory factor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:CAFA.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:CAFA.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:CAFA.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:0002830; P:positive regulation of type 2 immune response; IBA:GO_Central.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:CAFA.
DR GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0070206; P:protein trimerization; IEA:InterPro.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0043030; P:regulation of macrophage activation; NAS:UniProtKB.
DR GO; GO:0034341; P:response to type II interferon; IDA:UniProtKB.
DR GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
DR GO; GO:0045058; P:T cell selection; NAS:UniProtKB.
DR CDD; cd00191; TY; 1.
DR Gene3D; 1.10.870.10; MHC class II-associated invariant chain, trimerisation domain; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR InterPro; IPR043530; CD74_antigen.
DR InterPro; IPR015386; MHC_II-assoc_invar/CLIP_MHC-bd.
DR InterPro; IPR022339; MHC_II-assoc_invar_chain.
DR InterPro; IPR011988; MHC_II-assoc_invariant_trimer.
DR InterPro; IPR036613; MHCII_invariant_trimer_sf.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR14093; HLA CLASS II GAMMA CHAIN; 1.
DR PANTHER; PTHR14093:SF17; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN; 1.
DR Pfam; PF09307; MHC2-interact; 1.
DR Pfam; PF08831; MHCassoc_trimer; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PIRSF; PIRSF001992; CD74_antigen; 1.
DR PRINTS; PR01990; CD74ANTIGEN.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF48305; Class II MHC-associated invariant chain ectoplasmic trimerization domain; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative initiation;
KW Alternative splicing; Cell membrane; Chaperone; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Golgi apparatus; Immunity; Lysosome; Membrane; Phosphoprotein;
KW Proteoglycan; Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..296
FT /note="HLA class II histocompatibility antigen gamma chain"
FT /id="PRO_0000067954"
FT PEPTIDE 97..120
FT /note="Class-II-associated invariant chain peptide"
FT /evidence="ECO:0000269|PubMed:1448172"
FT /id="PRO_0000448886"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..72
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 210..271
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..226
FT /note="Required for interaction with CTSL"
FT /evidence="ECO:0000305|PubMed:10022822,
FT ECO:0000305|PubMed:32855215"
FT REGION 263..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 208..209
FT /note="Breakpoint for translocation to form a CD74-ROS1
FT fusion protein"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04441"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 203
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:22171320,
FT ECO:0000269|PubMed:23234360"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10022822"
FT CARBOHYD 281
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 282
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:25326458,
FT ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313,
FT ECO:0000269|PubMed:37453717"
FT DISULFID 213..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:10022822"
FT DISULFID 243..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:10022822"
FT DISULFID 252..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:10022822"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform p41 and isoform p33)"
FT /evidence="ECO:0000303|PubMed:3104027"
FT /id="VSP_060904"
FT VAR_SEQ 148..160
FT /note="NADPLKVYPPLKG -> SHWNWRTRLLGWV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037869"
FT VAR_SEQ 161..296
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037870"
FT VAR_SEQ 209..272
FT /note="Missing (in isoform p35 and isoform p33)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:6324166,
FT ECO:0000303|PubMed:6586420, ECO:0000303|Ref.5"
FT /id="VSP_005331"
FT MUTAGEN 225..226
FT /note="PG->RR,DD: Decreases inhibition of Ebola virus
FT infection."
FT /evidence="ECO:0000269|PubMed:32855215"
FT MUTAGEN 225..226
FT /note="PG->TT: No effect on inhibition of Ebola virus
FT infection."
FT /evidence="ECO:0000269|PubMed:32855215"
FT CONFLICT 167
FT /note="R -> T (in Ref. 3; CAA27047)"
FT /evidence="ECO:0000305"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:1IIE"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:1IIE"
FT HELIX 175..194
FT /evidence="ECO:0007829|PDB:1IIE"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:1ICF"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1L3H"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1ICF"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:1ICF"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1ICF"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1ICF"
SQ SEQUENCE 296 AA; 33516 MW; 27A13F252D5FB91D CRC64;
MHRRRSRSCR EDQKPVMDDQ RDLISNNEQL PMLGRRPGAP ESKCSRGALY TGFSILVTLL
LAGQATTAYF LYQQQGRLDK LTVTSQNLQL ENLRMKLPKP PKPVSKMRMA TPLLMQALPM
GALPQGPMQN ATKYGNMTED HVMHLLQNAD PLKVYPPLKG SFPENLRHLK NTMETIDWKV
FESWMHHWLL FEMSRHSLEQ KPTDAPPKVL TKCQEEVSHI PAVHPGSFRP KCDENGNYLP
LQCYGSIGYC WCVFPNGTEV PNTRSRGHHN CSESLELEDP SSGLGVTKQD LGPVPM
//